MolNFT v1 · #39724 · protein

The structure of the class C acid phosphatase from bacillus anthracis

2I33: “The structure of the class C acid phosphatase from bacillus anthracis”. X-ray diffraction, 1 ligand (MG), 4 pockets (best druggability 0.69). MolNFT v1 #39724 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2I33
Type: protein
Length: 474 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acid phosphatase
EC: 3.1.3.2
UniProt: Q81L82
Ligands: MG
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acid phosphatase (EC 3.1.3.2)	protein	238	51% helix, 15% strand	Q81L82
B	Acid phosphatase (EC 3.1.3.2)	protein	236	51% helix, 15% strand	Q81L82

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	470	0.69	0.80	39	empty
2	399	0.67	0.81	43	MG
3	84	0.36	0.75	21	empty
4	87	0.32	0.73	23	empty

Interfaces

1 interface between chains.

A–B · 2902 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

2I33 · The structure of the Class C acid phosphatase from Bacillus anthracis · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q81L82
Elsewhere: RCSB PDB 2I33 · PDBe 2I33 · UniProt Q81L82

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